Cooperativity plays an important role in metabolic regulation by controling the rates of enzyme catalyzed reactions. Cooperativity may also be involved in the actual mechanisms of catalysis by coupling together out-of-phase reaction cycles. Two types of allosteric interactions have been proposed to explain cooperative ligand binding equilibria, and coupled conformational changes, in oligomeric enzymes. However, the full range of kinetic cooperative behavior which may result from these allosteric interactions has not been examined rigorously. As a result, certain cooperative phenomena, particularly the class of effects known as half-of-the-sites reactivity, may have been interpreted too narrowly. In particular, the possibility that positive equilibrium cooperativity may be accompanied by negative kinetic cooperativity and metastable behavior seems to have been generally overlooked. The general statistical mechanical approach, which we have used previously to study cooperativity in hemoglobin and glyceraldehyde-3-phosphate dehydrogenase, is ideally suited to a quantitative study of kinetic cooperativity. The equilibrim formulation of the general model extends readily to the kinetic situation if the master equation is used in conjuntion with absolute rate theory. This approach has the advantages of minimizing the number of parameters required while emphasizing the mechanisms, geometries and strengths of the interactions between subunits. In addition to their predictive value, the quantitative results which we may obtain may be used to analyze existing data in order to characterize the allosteric mechanisms responsible for the observed cooperative behavior of particular enzymes. Our results will also be used to explore possible mechanisms for reciprocating modes of catalytic activity in oligomeric enzymes and the significance that these may have for catalytic efficiency.